4G9H

Crystal structure of glutahtione s-transferase homolog from yersinia pestis, target EFI-501894, with bound glutathione

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	APS BEAMLINE 31-ID
Synchrotron site	APS
Beamline	31-ID
Temperature [K]	100
Detector technology	CCD
Collection date	2012-07-09
Detector	RAYONIX 225 HE
Wavelength(s)	0.9793
Spacegroup name	P 41 21 2
Unit cell lengths	87.945, 87.945, 148.786
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	34.770 - 2.100
R-factor	0.1779
Rwork	0.176
R-free	0.21640
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	2pmt
RMSD bond length	0.007
RMSD bond angle	1.019
Data reduction software	MOSFLM
Data scaling software	SCALA
Phasing software	PHENIX
Refinement software	PHENIX (1.8_1069)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	75.709	2.130
High resolution limit [Å]	2.100	2.100
Rmerge	0.107	0.791
Number of reflections	34816
<I/σ(I)>	14.8	3.2
Completeness [%]	99.9	99.8
Redundancy	9.6	9.7

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	sitting drop vapor diffuction	7.5	298	Protein (10 mM Hepes pH 7.5, 100 mM NaCl); Reservoir (0.6 M NaCl, 0.1 M MES pH 6.5, 20% Peg4000); Cryoprotection (Reservoir, + 20% glycerol), sitting drop vapor diffuction, temperature 298K